Solution structures of the double-stranded RNA-binding domains from rna helicase A

2012 ◽  
Vol 80 (6) ◽  
pp. 1699-1706 ◽  
Author(s):  
Takashi Nagata ◽  
Kengo Tsuda ◽  
Naohiro Kobayashi ◽  
Mikako Shirouzu ◽  
Takanori Kigawa ◽  
...  
Keyword(s):  
Rna Binding ◽  
Rna Helicase ◽  
Rna Helicase A ◽  
Double Stranded Rna ◽  
Solution Structures ◽  
Binding Domains ◽  
Rna Binding Domains

scholarly journals Features of Double-stranded RNA-binding Domains of RNA Helicase A Are Necessary for Selective Recognition and Translation of Complex mRNAs

2010 ◽  
Vol 286 (7) ◽  
pp. 5328-5337 ◽  
Author(s):  
Arnaz Ranji ◽  
Nikolozi Shkriabai ◽  
Mamuka Kvaratskhelia ◽  
Karin Musier-Forsyth ◽  
Kathleen Boris-Lawrie
Keyword(s):  
Rna Binding ◽  
Rna Helicase ◽  
Selective Recognition ◽  
Rna Helicase A ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
Rna Binding Domains

scholarly journals RNA Helicase A Regulates the Replication of RNA Viruses

Viruses ◽  
2021 ◽  
Vol 13 (3) ◽  
pp. 361
Author(s):  
Rui-Zhu Shi ◽  
Yuan-Qing Pan ◽  
Li Xing
Keyword(s):  
Virus Replication ◽  
Rna Binding ◽  
Rna Viruses ◽  
Rna Helicase ◽  
Rna Helicase A ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
N Terminus

The RNA helicase A (RHA) is a member of DExH-box helicases and characterized by two double-stranded RNA binding domains at the N-terminus. RHA unwinds double-stranded RNA in vitro and is involved in RNA metabolisms in the cell. RHA is also hijacked by a variety of RNA viruses to facilitate virus replication. Herein, this review will provide an overview of the role of RHA in the replication of RNA viruses.

scholarly journals Double-stranded RNA-activated protein kinase PKR of fishes and amphibians: Varying the number of double-stranded RNA binding domains and lineage-specific duplications

BMC Biology ◽  
2008 ◽  
Vol 6 (1) ◽  
Author(s):  
Stefan Rothenburg ◽  
Nikolaus Deigendesch ◽  
Madhusudan Dey ◽  
Thomas E Dever ◽  
Loubna Tazi
Keyword(s):  
Protein Kinase ◽  
Rna Binding ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
Rna Binding Domains

scholarly journals Recognition of viral RNA stem-loops by the tandem double-stranded RNA binding domains of PKR

RNA ◽  
2013 ◽  
Vol 19 (3) ◽  
pp. 333-344 ◽  
Author(s):  
E. Dzananovic ◽  
T. R. Patel ◽  
S. Deo ◽  
K. McEleney ◽  
J. Stetefeld ◽  
...  
Keyword(s):  
Rna Binding ◽  
Viral Rna ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
Rna Binding Domains

scholarly journals The N-Terminal Double-Stranded RNA Binding Domains of Arabidopsis HYPONASTIC LEAVES1 Are Sufficient for Pre-MicroRNA Processing

2007 ◽  
Vol 19 (3) ◽  
pp. 914-925 ◽  
Author(s):  
Feijie Wu ◽  
Lin Yu ◽  
Wenguang Cao ◽  
Yanfei Mao ◽  
Zhongyuan Liu ◽  
...  
Keyword(s):  
Rna Binding ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
Microrna Processing ◽  
Rna Binding Domains

scholarly journals RNA recognition by double-stranded RNA binding domains: a matter of shape and sequence

2012 ◽  
Author(s):  
Grégoire Masliah ◽  
Pierre Barraud ◽  
Frédéric H. -T. Allain
Keyword(s):  
Rna Binding ◽  
Rna Recognition ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
Rna Binding Domains

scholarly journals Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless

2018 ◽  
Author(s):  
Pravin Kumar Ankush Jagtap ◽  
Marisa Müller ◽  
Pawel Masiewicz ◽  
Sören von Bülow ◽  
Nele Merret Hollmann ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Motifs ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
Dsrna Binding ◽  
Rna Binding Domains ◽  
Human Orthologue ◽  
Rox Rna

ABSTRACTMaleless (MLE) is an evolutionary conserved member of the DExH family of helicases in Drosophila. Besides its function in RNA editing and presumably siRNA processing, MLE is best known for its role in remodelling non-coding roX RNA in the context of X chromosome dosage compensation in male flies. MLE and its human orthologue, DHX9 contain two tandem double-stranded RNA binding domains (dsRBDs) located at the N-terminal region. The two dsRBDs are essential for localization of MLE at the X-territory and it is presumed that this involves binding roX secondary structures. However, for dsRBD1 roX RNA binding has so far not been described. Here, we determined the solution NMR structure of dsRBD1 and dsRBD2 of MLE in tandem and investigated its role in double-stranded RNA (dsRNA) binding. Our NMR data show that both dsRBDs act as independent structural modules in solution and are canonical, non-sequence-specific dsRBDs featuring non-canonical KKxAK RNA binding motifs. NMR titrations combined with filter binding experiments document the contribution of dsRBD1 to dsRNA binding in vitro. Curiously, dsRBD1 mutants in which dsRNA binding in vitro is strongly compromised do not affect roX2 RNA binding and MLE localization in cells. These data suggest alternative functions for dsRBD1 in vivo.

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